The events controlling cell division are governed by the degradation of different
regulatory proteins by the Ubiquitin-dependent pathway.
Ubiquitin, a small protein of 76 amino acids is found in all
eukaryotic cells. In the Ubiquitin-dependent pathway, the
attachment of a polyubiquitin chain to a substrate is realized by an ubiquitin-ligase
targets this substrate for degradation by the 26S proteasome. The ubiquitination pathway
sequentially involves the E1 Ub-activating enzyme, E2 Ub-conjugating enzymes, and E3
Ub-ligases [1].

SCF complex participates in cell cycle regulation by
stimulating ubiquitination of the cell cycle proteins and their degradation by the 26S
proteasome. Most substrates require phosphorylation to interact with the F-box protein in
an SCF complex [1].

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